The estrogen receptor alpha (ERa), a transcription factor that controls the expression of a number of genes involved in cellular differentiation and proliferation in a wide variety of tissues, is regulated by ligand binding and phosphorylation. ER contains at least two transcriptionally active domains: constitutively active F-1 at the ER N-terminus of the protein and ligand-dependent AF-2 at the ER C-terminus. Although ligand binding is considered essential for the full activation of ER, it has long been recognized that the receptor is subject to post-translational alterations, such as phosphorylation, which also regulated its activity. ER phosphorylation patterns appear to be cell type-specific. Serine 167 has been shown to be phosphorylated by p90rsk1 in vitro and to regulate ER AF-1-dependent transcriptional activation in vivo.

Catalog #

E3565-12A

Applications

Suitable for use in Western Blot. Other applications not tested.

Recommended Dilution

Western Blot: 0.5-2ug/ml

Optimal dilutions to be determined by the researcher.

Storage and Stability

May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

Clone Type

Polyclonal

Isotype

IgG

Host

Rabbit

Source

Human

Concentration

~0.1mg/ml

Form

Supplied as a liquid in PBS, pH 7.4, 0.05% sodium azide.

Purity

Purified by immunoaffinity chromatography.

Immunogen

Synthetic peptide (RLApSTND) corresponding to human ER at the phosphorylated site of Serine 167.

Specificity

Recognizes human ER alpha. Species Crossreactivity: mouse and rat.

Important Note

This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.